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1 phate (PLP) to isomerize L-alpha-lysine to L-beta-lysine.
2 e terminal amino group of dl-lysine and of l-beta-lysine.
3 o group of a substrate, either D-lysine or L-beta-lysine.
4 alyzes the interconversion of L-lysine and L-beta-lysine.
5  the interconversion of l-alpha-lysine and l-beta-lysine.
6 alyzes the interconversion of L-lysine and L-beta-lysine.
7 ons of 5,6-LAM with D- or L-lysine or with L-beta-lysine.
8 alyzes the interconversion of l-lysine and l-beta-lysine.
9 xanoate, as well as the interconversion of L-beta-lysine and l-3,5-diaminohexanoate.
10 then abstracts an H-atom from 5'-Ado to form beta-lysine and the 5'-deoxyadenosyl radical; the latter
11 acterial elongation factor P (EF-P) with (R)-beta-lysine at a conserved lysine residue activates the
12 alyzes the interconversion of l-lysine and l-beta-lysine by a free radical mechanism.
13 es the interconversion of (S)-lysine and (S)-beta-lysine by a radical mechanism involving coenzymatic
14  in the isomerization of L-alpha-lysine to L-beta-lysine by LAM, via the stable allylic anhydroadenos
15 res post-translational modification with (R)-beta-lysine by the lysyl-tRNA synthetase paralog PoxA.
16 ism of the interconversion of L-lysine and L-beta-lysine catalyzed by lysine 2,3-aminomutase (LAM) in
17                    The alternative substrate beta-lysine induces inactivation at least 25 times faste
18                                    While (S)-beta-lysine is not a substrate for E. coli LAM, it under
19 wo-step reaction involving the addition of a beta-lysine moiety and the subsequent hydroxylation, cat
20                                          The beta-lysine moiety was previously shown to enhance the r
21 ndergoes hydrogen abstraction to form an (S)-beta-lysine-related radical with the same stereochemistr
22                                              Beta-lysine-related radicals are observed in the reactio
23           Moreover, the conformations of the beta-lysine-related radicals at the active sites of E. c
24     The product of the E. coli enzyme is (R)-beta-lysine, the enantiomer of the clostridial product.
25 alyzes the interconversion of L-lysine and L-beta-lysine, the first step in lysine degradation in Clo
26 odified by PoxA, which covalently attaches a beta-lysine to a conserved lysine residue of EF-P.
27 hemistry of hydrogen transfer from C2 of (S)-beta-lysine to the 5'-deoxyadenosyl radical as in the ac
28  D-lysine with 2,5-diaminohexanoate and of L-beta-lysine with 3,5-diaminohexanoate.

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